Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6H5N

Plasmodium falciparum Pfs48/45 C-terminal domain bound to monoclonal antibody 85RF45.1

Summary for 6H5N
Entry DOI10.2210/pdb6h5n/pdb
DescriptorGametocyte surface protein P45/48, Antibody 85RF45.1 light chain, Antibody 85RF45.1 heavy chain (3 entities in total)
Functional Keywordspfs48/45 gamete fusion plasmodium falciparum transmission blocking monoclonal antibody, cell invasion
Biological sourcePlasmodium falciparum (isolate 3D7)
More
Total number of polymer chains6
Total formula weight124270.55
Authors
Lennartz, F.,Higgins, M.K. (deposition date: 2018-07-25, release date: 2018-09-26, Last modification date: 2024-11-13)
Primary citationLennartz, F.,Brod, F.,Dabbs, R.,Miura, K.,Mekhaiel, D.,Marini, A.,Jore, M.M.,Sogaard, M.M.,Jorgensen, T.,de Jongh, W.A.,Sauerwein, R.W.,Long, C.A.,Biswas, S.,Higgins, M.K.
Structural basis for recognition of the malaria vaccine candidate Pfs48/45 by a transmission blocking antibody.
Nat Commun, 9:3822-3822, 2018
Cited by
PubMed Abstract: The quest to develop an effective malaria vaccine remains a major priority in the fight against global infectious disease. An approach with great potential is a transmission-blocking vaccine which induces antibodies that prevent establishment of a productive infection in mosquitos that feed on infected humans, thereby stopping the transmission cycle. One of the most promising targets for such a vaccine is the gamete surface protein, Pfs48/45. Here we establish a system for production of full-length Pfs48/45 and use this to raise a panel of monoclonal antibodies. We map the binding regions of these antibodies on Pfs48/45 and correlate the location of their epitopes with their transmission-blocking activity. Finally, we present the structure of the C-terminal domain of Pfs48/45 bound to the most potent transmission-blocking antibody, and provide key molecular information for future structure-guided immunogen design.
PubMed: 30237518
DOI: 10.1038/s41467-018-06340-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.23 Å)
Structure validation

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon